23LY

Crystal structure of SARS-CoV-2 main protease E166V mutant in complex with leritrelvir

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SSRF BEAMLINE BL19U1
Synchrotron site	SSRF
Beamline	BL19U1
Temperature [K]	100
Detector technology	PIXEL
Collection date	2024-09-08
Detector	DECTRIS PILATUS3 6M
Wavelength(s)	0.97923
Spacegroup name	P 1 21 1
Unit cell lengths	48.837, 106.317, 54.145
Unit cell angles	90.00, 103.22, 90.00

Refinement procedure

Resolution	53.159 - 1.560
Rwork	0.147
R-free	0.19740
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.009
RMSD bond angle	1.800
Data reduction software	XDS (BUILT 20240630)
Data scaling software	Aimless (0.7.7)
Phasing software	PHASER (2.8.3)
Refinement software	REFMAC (5.8.0430)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	53.160	1.590
High resolution limit [Å]	1.560	1.560
Rmerge	0.076	0.859
Number of reflections	76106	3784
<I/σ(I)>	12.2	2.4
Completeness [%]	99.7
Redundancy	5.2
CC(1/2)	0.997	0.615

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP		289	0.1 M Ammonium citrate tribasic pH 6.0, 14% w/v Polyethylene glycol 3350